Premium
Structure prediction, evolution and ligand interaction of CHASE domain
Author(s) -
Pas Jakub,
von Grotthuss Marcin,
Wyrwicz Lucjan S.,
Rychlewski Leszek,
Barciszewski Jan
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.09.020
Subject(s) - histidine , histidine kinase , signal transduction , biochemistry , receptor , biology , microbiology and biotechnology , homology (biology) , kinase , extracellular , protein domain , chemistry , biophysics , amino acid , gene
Cytokinins are plant hormones involved in the essential processes of plant growth and development. They bind with receptors known as CRE1/WOL/AHK4, AHK2, and AHK3, which possess histidine kinase activity. Recently, the sensor domain cyclases/histidine kinases associated sensory extracellular (CHASE) was identified in those proteins but little is known about its structure and interaction with ligands. Distant homology detection methods developed in our laboratory and molecular phylogeny enabled the prediction of the structure of the CHASE domain as similar to the photoactive yellow protein‐like sensor domain. We have identified the active site pocket and amino acids that are involved in receptor–ligand interactions. We also show that fold evolution of cytokinin receptors is very important for a full understanding of the signal transduction mechanism in plants.